TY - JOUR
T1 - Characterization of Three Types of Turban Shell Batillus cornutus Muscle—Ultrastructure and Protein Composition
AU - Watabe, Shugo
AU - Ochiai, Yoshihiro
AU - Kariya, Yutaka
AU - Dinh, Thi Ngoc Loan
AU - Hashimoto, Kanehisa
AU - Kimura, Shigeru
AU - Pyeung, Jae Hyeun
PY - 1986
Y1 - 1986
N2 - Three types of turban shell Batillus cornutus muscle—foot, opercular and visceral—were examined under an electron microscope, and the results discussed in association with their differences in muscle protein composition. Myofibrils of foot muscle were partially surrounded by a collagen fibril layer of about 1 μm thickness. Diameters of thick filaments fell in a wide range of 22–70 nm (mean value, 50 nm). The myofibrils were found to be crossing each other at right angles. The opercular muscle showed a similar structure, except that the collagen fibril layer was clearly thinner. The visceral muscle which surrounds the viscera was composed of roughly parallel-running myofibrils whose thick filaments had a mean diameter of 50 nm. Paramyosin contents in the myofibrillar protein were 29–41 % through the three types of muscle. The paramyosin to myosin heavy chain ratios were 2.5 and 2.3 in the foot and opercular muscles, respectively, whereas the ratio in the visceral muscle was 1.4. The collagen to crude protein ratio was 45% in the foot, 34% in the opercular and 5% in the visceral muscle, roughly agreeing with their electron microscopic differences.
AB - Three types of turban shell Batillus cornutus muscle—foot, opercular and visceral—were examined under an electron microscope, and the results discussed in association with their differences in muscle protein composition. Myofibrils of foot muscle were partially surrounded by a collagen fibril layer of about 1 μm thickness. Diameters of thick filaments fell in a wide range of 22–70 nm (mean value, 50 nm). The myofibrils were found to be crossing each other at right angles. The opercular muscle showed a similar structure, except that the collagen fibril layer was clearly thinner. The visceral muscle which surrounds the viscera was composed of roughly parallel-running myofibrils whose thick filaments had a mean diameter of 50 nm. Paramyosin contents in the myofibrillar protein were 29–41 % through the three types of muscle. The paramyosin to myosin heavy chain ratios were 2.5 and 2.3 in the foot and opercular muscles, respectively, whereas the ratio in the visceral muscle was 1.4. The collagen to crude protein ratio was 45% in the foot, 34% in the opercular and 5% in the visceral muscle, roughly agreeing with their electron microscopic differences.
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U2 - 10.2331/suisan.52.737
DO - 10.2331/suisan.52.737
M3 - Article
AN - SCOPUS:85008100665
VL - 52
SP - 737
EP - 744
JO - Nippon Suisan Gakkaishi
JF - Nippon Suisan Gakkaishi
SN - 0021-5392
IS - 4
ER -